Bottom Line:
As-p18 is a fatty-acid-binding protein from the parasitic nematode Ascaris suum.Although it exhibits sequence similarity to mammalian intracellular fatty-acid-binding proteins, it contains features that are unique to nematodes.Crystals were obtained, but initial diffraction data analysis revealed that they were composed of a number of `microdomains'.

Affiliation: Institute of Infection, Immunity and Inflammation, University of Glasgow, Glasgow, Scotland. mgabr@chem.gla.ac.uk

ABSTRACTAs-p18 is a fatty-acid-binding protein from the parasitic nematode Ascaris suum. Although it exhibits sequence similarity to mammalian intracellular fatty-acid-binding proteins, it contains features that are unique to nematodes. Crystals were obtained, but initial diffraction data analysis revealed that they were composed of a number of `microdomains'. Interpretable data could only be collected using a microfocus beamline with a beam size of 12 × 8 µm.

Mentions:
Protein crystals appeared within two weeks in condition No. 2 (40% ethylene glycol, 0.1 M acetate pH 4.5) of the Cryo I screen (Emerald BioSystems, USA). The largest crystals had maximum dimensions of 0.08 × 0.08 × 0.1 mm (Fig. 1 ▶). Crystals were cooled without any additional cryoprotection in a stream of gaseous nitrogen cooled to 100 K (Oxford Cryosystems, England) and were stored under liquid nitrogen until diffraction testing.

Bottom Line:
As-p18 is a fatty-acid-binding protein from the parasitic nematode Ascaris suum.Although it exhibits sequence similarity to mammalian intracellular fatty-acid-binding proteins, it contains features that are unique to nematodes.Crystals were obtained, but initial diffraction data analysis revealed that they were composed of a number of `microdomains'.

Affiliation:
Institute of Infection, Immunity and Inflammation, University of Glasgow, Glasgow, Scotland. mgabr@chem.gla.ac.uk

ABSTRACTAs-p18 is a fatty-acid-binding protein from the parasitic nematode Ascaris suum. Although it exhibits sequence similarity to mammalian intracellular fatty-acid-binding proteins, it contains features that are unique to nematodes. Crystals were obtained, but initial diffraction data analysis revealed that they were composed of a number of `microdomains'. Interpretable data could only be collected using a microfocus beamline with a beam size of 12 × 8 µm.